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<p>RNase MRP is a conserved eukaryotic ribonucleoprotein essential for precursor-rRNA processing and ribosome assembly. Despite previous studies of yeast RNase MRP, the composition of RNase MRP and how it adapts to process flexible, single-stranded rRNA substrates in most eukaryotes remain enigmatic. Here, we perform an integrative structural, evolutionary, and functional dissection of human RNase MRP. Using structure-based bioinformatics and cryo-EM structural analyses, we identify NEPRO (RMP64) and C18orf21 (RMP24) as the bona fide subunits unique to RNase MRP, which are indispensable for precursor-rRNA cleavage, ribosome assembly, protein synthesis, and chondrogenesis. The structure of human RNase MRP reveals a unique ‘double-anchor’ substrate-binding mechanism that underlies evolutionary adaptations conferring broad substrate specificity. Our work on RNase MRP provides a unified evolutionary and mechanistic framework for this essential ancient ribozyme.</p>

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Structural and evolutionary insights into the eukaryotic RNase MRP ribonucleoprotein complex

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年3月26日

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  • Bin Zhou,
  • Xiaozhu Wang,
  • Futang Wan,
  • Shaobai Li,
  • Xiaoshuang Zhang,
  • Yuanyuan Zhang,
  • Ming Tan,
  • Mi Cao,
  • Yafeng Shen,
  • Rui Gao,
  • Yanjie Zhang,
  • Pengfei Lan,
  • Jian Wu,
  • Ming Lei

摘要

RNase MRP is a conserved eukaryotic ribonucleoprotein essential for precursor-rRNA processing and ribosome assembly. Despite previous studies of yeast RNase MRP, the composition of RNase MRP and how it adapts to process flexible, single-stranded rRNA substrates in most eukaryotes remain enigmatic. Here, we perform an integrative structural, evolutionary, and functional dissection of human RNase MRP. Using structure-based bioinformatics and cryo-EM structural analyses, we identify NEPRO (RMP64) and C18orf21 (RMP24) as the bona fide subunits unique to RNase MRP, which are indispensable for precursor-rRNA cleavage, ribosome assembly, protein synthesis, and chondrogenesis. The structure of human RNase MRP reveals a unique ‘double-anchor’ substrate-binding mechanism that underlies evolutionary adaptations conferring broad substrate specificity. Our work on RNase MRP provides a unified evolutionary and mechanistic framework for this essential ancient ribozyme.